eF-site ID 4qwu-K PDB Code 4qwu Chain K click to enlarge Title yCP beta5-C52F mutant in complex with bortezomib Classification HYDROLASE/HYDROLASE INHIBITOR Compound Proteasome subunit alpha type-2 Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence K:  TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPF LLGTMAGGAADFQFWETWLGSQCRLHELREKERISVAAAS KILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGT RLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRS ILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKV KEEEGSFNNVIG Description Functional site 1) chain K residue 1 type sequence T description BINDING SITE FOR RESIDUE BO2 K 301 source : AC5 2) chain K residue 20 type sequence A description BINDING SITE FOR RESIDUE BO2 K 301 source : AC5 3) chain K residue 21 type sequence T description BINDING SITE FOR RESIDUE BO2 K 301 source : AC5 4) chain K residue 45 type sequence M description BINDING SITE FOR RESIDUE BO2 K 301 source : AC5 5) chain K residue 47 type sequence G description BINDING SITE FOR RESIDUE BO2 K 301 source : AC5 6) chain K residue 48 type sequence G description BINDING SITE FOR RESIDUE BO2 K 301 source : AC5 7) chain K residue 49 type sequence A description BINDING SITE FOR RESIDUE BO2 K 301 source : AC5 8) chain K residue 170 type sequence Y description BINDING SITE FOR RESIDUE BO2 K 301 source : AC5 9) chain K residue 165 type sequence A description BINDING SITE FOR RESIDUE MG K 302 source : AC6 10) chain K residue 166 type sequence H description BINDING SITE FOR RESIDUE MG K 302 source : AC6 11) chain K residue 168 type sequence D description BINDING SITE FOR RESIDUE MG K 302 source : AC6 12) chain K residue 171 type sequence S description BINDING SITE FOR RESIDUE MG K 302 source : AC6 13) chain K residue 4-51 type prosite sequence LAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLG TMAGGAAD description PROTEASOME_BETA_1 Proteasome beta-type subunits signature. VGVkFnnGVVIAADtrstqgpivadknca.KlhrispkiwcagaGtaAD source prosite : PS00854 14) chain K residue 49 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI2

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